Abstract
The aim of this work was to study the contribution of the N-terminal structure to cellulase catalytic performance. A wild-type cellulase (BaCel5) of glycosyl hydrolase (GH) family 5 from Bispora antennata and two hybrid enzymes (BaCel5127 and BaCel5167) with replacement of the N-terminal (βα)3 (127 residues) or (βα)4 (167 residues)-barrel with the corresponding sequences of TeEgl5A from Talaromyces emersonii were produced in Pichia pastoris and biochemically characterized. BaCel5 exhibited optimal activity at pH 5.0 and 50°C but had low catalytic efficiency (25.4±0.8mLs−1mg−1). In contrast, BaCel5127 and BaCel5167 showed similar enzymatic properties but improved catalytic performance. When using CMC-Na, barley β-glucan, lichenan, and cellooligosaccharides as substrates, BaCel5127 and BaCel5167 had increased specific activities and catalytic efficiencies by ∼1.8−6.7-fold and ∼1.0−4.7-fold, respectively. The catalytic efficiency of BaCel5167 was even higher than that of parental proteins. The underlying mechanism was analyzed by molecular docking and molecular dynamic simulation.
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